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A more recent version of this article appeared on July 1, 2004
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Submitted on May 23, 2003
Revised on March 30, 2004
Accepted on April 9, 2004
1 INIMEC-CONICET, 5000 Cordoba, Argentina
2 Division of Biochemistry, Osaka University Medical School, Suita, Osaka 565-0871, Japan
3 CIQUIBIC-CONICET, 5000 Cordoba, Argentina
4 Institute for Neuroscience and Department of Cell and Molecular Biology, Northwestern University, Chicago, IL 60611
* Corresponding author. E-mail address: acaceres{at}immf.uncor.edu.
In this study we examined the subcellular distribution and functions of LIMK1 in developing neurons. Confocal microscopy, subcellular fractionation, and expression of several epitope-tagged LIMK1 constructs revealed that LIMK1 is enriched in the Golgi apparatus and growth cones, with the LIM domain required for Golgi localization and the PDZ domain for its presence at neuritic tips. Overexpression of wild-type LIMK1 suppresses the formation of trans-Golgi derived tubules, and prevents cytochalasin D-induced Golgi fragmentation, while that of a kinase-defective mutant has the opposite effect. Transfection of wild-type LIMK1 accelerates axon formation and enhances the accumulation of Par3/Par6, IGF1 receptors, and NCAM at growth cones, while inhibiting the Golgi export of synaptophysin-containing vesicles. These effects were dependent on the Golgi localization of LIMK1, paralleled by an increase in cofilin phosphorylation and phalloidin staining in the region of the Golgi apparatus, and prevented by coexpression of constitutive active cofilin. The long-term overexpression of LIMK1 produces growth cone collapse and axon retraction, an effect that is dependent on its growth cone localization. Taken together, our results suggest an important role for LIMK1 in axon formation that is related with its ability to regulate Golgi dynamics, membrane traffic, and actin cystokeletal organization.
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